9LUX

Single-chain Fv antibody of G2 fused with antigen peptide from chicken prion protein

Summary for 9LUX

• Entry DOI: 10.2210/pdb9lux/pdb
• Descriptor: Major prion protein homolog,Single-chain Fv antibody of G2 fused with antigen peptide from chicken prion protein, SULFATE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: antigen binding, affinity maturation, somatic hypermutation, immune system
• Biological source: Gallus gallus (chicken); More
• Total number of polymer chains: 6
• Total formula weight: 174651.20

Authors

Hanazono, Y.,Yabuno, S.,Hayashi, T.,Numoto, N.,Ito, N.,Oda, M. (deposition date: 2025-02-10, release date: 2025-06-11, Last modification date: 2025-07-02)

Primary citation

Hanazono, Y.,Yabuno, S.,Hayashi, T.,Numoto, N.,Kamatari, Y.O.,Ito, N.,Oda, M.
Crystal structures reveal how the multispecific antibody G2 achieves binding to different peptides.
Febs Lett., 2025

PubMed Abstract: Monoclonal antibody G2, obtained via immunization with the chicken prion protein (ChPrP), has unique antigen-binding specificity. G2 specifically binds to the ChPrP-derived peptide (Pep18mer) as expected, but also to three other peptides. In this study, we determined the crystal structures of G2 single-chain Fv antibodies covalently linked to Pep18mer and another peptide, PepH4P6. Both bound peptides formed similar U-shaped structures that stuck into the G2 antigen-binding pocket. Their three-dimensional structures were stabilized by interactions within the peptides, and the structure of the bound Pep18mer was similar to that of the corresponding ChPrP region. G2 acquired the binding ability to both Pep18mer and PepH4P6 via deletion of the 95th residue of the light chain during affinity maturation, consistent with our structural analysis.

PubMed: 40527602
DOI: 10.1002/1873-3468.70095

Experimental method

X-RAY DIFFRACTION (1.85 Å)